Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta' (A5N4P0)
Analyse AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta'… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5N4P0
- Type
- protein
- Length
- 1,174 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x923014Dfc95D087762F5F4fb0e38d445B684DB83
- Molecule
- DNA-directed RNA polymerase subunit beta'
- UniProt
- A5N4P0
- Pockets
- 18 · best druggability 0.73
Structure
1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta' | protein | 1174 | 45% helix, 16% strand | A5N4P0 |
Pockets
18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.73 | 0.92 | 25 | empty |
| 2 | 634 | 0.70 | 0.77 | 46 | empty |
| 3 | 759 | 0.68 | 0.75 | 46 | empty |
| 4 | 861 | 0.68 | 0.74 | 64 | empty |
| 5 | 420 | 0.59 | 0.75 | 47 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A5N4P0
- Elsewhere: UniProt A5N4P0 · AlphaFold DB A5N4P0
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